With poly(ethylene glycol) diacrylate as the cross-linker and the further modification of gold nanoparticles, the matrix has advantages of good hydrophilicity and enhanced surface area, which are beneficial to improve the enrichment selectivity and efficiency for glycoproteins. Herein, we report a new kind of hydrophilic boronate affinity monolith by attaching 4- mercaptophenylboronic acid (MPBA) with 2-mercaptoethylamine (MPA) on the gold nanoparticle-modified poly(glycidyl methacrylate-co-poly(ethylene glycol) diacrylate)) monolith for glycoprotein enrichment. As a result, 160 glycoproteins were credibly identified from 9 μg of human plasma, demonstrating the great potential of such a monolith for large-scale glycoproteome research.ĪB - As low abundance is the great obstacle for glycoprotein analysis, the development of materials with high efficiency and selectivity for glycoprotein enrichment is a prerequisite in glycoproteome research. Finally, the boronate affinity monolith was successfully applied for the human-plasma glycoproteome analysis. Furthermore, the average recovery of HRP on the prepared affinity monoliths was (84.8☑.9) %, obtained in three times enrichment with the same column. In addition, the binding capacity of ovalbumin on such monolith reached 390 μg g-1. Such a boronate affinity monolith was applied to enrich horseradish peroxidase (HRP) from the mixture of HRP and bovine serum albumin (BSA), and high selectivity was obtained even at a mass ratio of 1:1000. The attachment of MPBA and MPA provide intramolecular B-N coordination, which could further enhance the specificity of glycoprotein capture. N2 - As low abundance is the great obstacle for glycoprotein analysis, the development of materials with high efficiency and selectivity for glycoprotein enrichment is a prerequisite in glycoproteome research. T1 - Boronate affinity monolith with a gold nanoparticle-modified hydrophilic polymer as a matrix for the highly specific capture of glycoproteins As a result, 160 glycoproteins were credibly identified from 9 μg of human plasma, demonstrating the great potential of such a monolith for large-scale glycoproteome research.",
Abstract = "As low abundance is the great obstacle for glycoprotein analysis, the development of materials with high efficiency and selectivity for glycoprotein enrichment is a prerequisite in glycoproteome research.
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